(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y378_YERPA

ID   A0A0H2Y378_YERPA        Unreviewed;       291 AA.
AC   A0A0H2Y378;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   RecName: Full=Glutamate racemase {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00524481};
DE            EC=5.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00358505};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN   OrderedLocusNames=YPA_0113 {ECO:0000313|EMBL:ABG12082.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12082.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12082.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12082.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00258,
CC       ECO:0000256|SAAS:SAAS00551341}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00258,
CC         ECO:0000256|SAAS:SAAS01120479};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00041181}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258, ECO:0000256|SAAS:SAAS00571648}.
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DR   EMBL; CP000308; ABG12082.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12082; ABG12082; YPA_0113.
DR   KEGG; ypa:YPA_0113; -.
DR   KO; K01776; -.
DR   OMA; VYGCTHY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00258; Glu_racemase; 1.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR   InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR   InterPro; IPR004391; Glu_race.
DR   PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2Y378.
DR   SWISS-2DPAGE; A0A0H2Y378.
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436155};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00041303};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00090451, ECO:0000313|EMBL:ABG12082.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258,
KW   ECO:0000256|SAAS:SAAS00436203}.
FT   REGION       36     37       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION       68     69       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      101    102       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   REGION      213    214       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00258}.
FT   ACT_SITE    100    100       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE    212    212       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00258}.
SQ   SEQUENCE   291 AA;  31887 MW;  682E6CC99E5EBDBF CRC64;
     MRWFMATKPQ DANTTSREAI TSKADSPPRP TALIFDSGVG GLSVYQEIRQ LLPDLHYIYA
     FDNVAFPYGE KSGEFIVERV LEIVTAVQQR HPLAIVVIAC NTASTVSLPA LRERFAFPVV
     GVVPAIKPAV RLTRNGVVGL LATRATVHAS YTLDLIARFA TDCKIELLGS SELVEVAETK
     LHGGVVPLEV LKKILHPWLS MREPPDTIVL GCTHFPLLTE ELAQVLPEGT RMVDSGAAIA
     RRTAWLISSQ ENVISSQDEN IAYCMALDED TDALLPVLQS YGFPKLQKLP I
//

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